ID A0A2K3UW20_9DEIO Unreviewed; 958 AA.
AC A0A2K3UW20;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN Name=sucA {ECO:0000313|EMBL:PNY80716.1};
GN ORFNames=CVO96_04455 {ECO:0000313|EMBL:PNY80716.1};
OS Deinococcus koreensis.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2054903 {ECO:0000313|EMBL:PNY80716.1, ECO:0000313|Proteomes:UP000236379};
RN [1] {ECO:0000313|EMBL:PNY80716.1, ECO:0000313|Proteomes:UP000236379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJW1-2 {ECO:0000313|EMBL:PNY80716.1,
RC ECO:0000313|Proteomes:UP000236379};
RA Choi A.;
RT "Deinococcus koreensis sp. nov., a radiation-resistant bacterium isolated
RT from river water.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNY80716.1}.
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DR EMBL; PPPD01000001; PNY80716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3UW20; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000236379; Unassembled WGS sequence.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:PNY80716.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236379};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 594..791
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 958 AA; 104775 MW; F705B04576C17F87 CRC64;
MLGGVMTVSQ TIMSGANAAF IEGLYEAYLA DPQSVDAGWR AYFDQVRGGA PETAHSPIQR
AFYDLGQTRR GAAAPAGGAA QGMSGAQQAA GALITSYRVY GHISARSNPL RMRGLPVVPE
LTPEFYGLTE ADLQEHVRDG PFEGPLREVI AQLQETYCGT IGFEYNYLPA NERQWFQARI
EQGRGQGRHD LTPGERRRLM QKLTAAEGLE LYLRNKYPGV KRFGLEGGES FIPLVDRIIQ
QAGRAGVKEV VLGMAHRGRL NTLVNIFGKK PSDLFDEFDG KKKISDDPDV AGDVKYHMGF
SSDVRTPGGA MHLAMAFNPS HLEIVSPVVH GSVRARQDRR GDTERRTVLP ITVHGDAAVS
GQGVVMETLN LSRLRGFATG GAVRIVINNQ IGFTISDPRD TRSSRYCTDI AKVANAPVLH
VNGDDPEAVA FCGDLAVAYR QEFGKDVFID LIGFRRNGHN EGDEPRMTQP IMYREIDQHP
GARAIYAKAL EESGVLAPGE GDALVAKFRD QLDAGESVVE EMENLAQSAL AVDWKSYTDT
HWDRDGVSTA VPVEKLTELG LKLAAVPEGF KVHRTIERTV IGPREAMARG EQPLDWGMGE
MLAYASLLDE GYGVRLVGQD SGRGTFVHRH AVLHDQNAAD PLNEEYMALA HLREGQGRVE
VVDSTLSEEA VLAFEYGYST SEPKGLVAWE AQFGDFANGA QAVVDQFLSA GESKWQRLSG
LVMLLPHGYE GAGPEHSSAR LERYLQLCAQ KNMQVVVPSS SAQIFHLLRR QVLRPYRKPL
IVMTPKSLLR NKQAMSPLNE LSGGRFQEVI GDPEVQKARR VVISSGKLHW ELAEARDADR
DGYAGTALIR LEQLYPFPAD ALSAELAAHP GAQVVWAQEE PQNQGAWLMI WEDLERVLAP
GQTLSSATRA RSASTATGYA SVHAREQAAV IATALGEPVQ KEVIQEQKEL AQTAQQDG
//